Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes (Q27640093)

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English	Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes	scientific article

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scholarly article

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Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes (English)

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crystal structure

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Ilme Schlichting

3

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author name string

Roman Fedorov

1

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Dipak K Ghosh

2

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language of work or name

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publication date

1 January 2003

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Archives of Biochemistry and Biophysics

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409

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1

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25-31

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Heme-Containing Oxygenases

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NO news is good news

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Neuronal nitric oxide synthase, a modular enzyme formed by convergent evolution: structure studies of a cysteine thiolate-liganded heme protein that hydroxylates L-arginine to produce NO. as a cellular signal.

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Nature's universal oxygenases: the cytochromes P450.

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Nitric oxide synthases: structure, function and inhibition

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Mechanism of nitric oxide synthase. Evidence that direct hydrogen atom abstraction from the O-H bond of NG-hydroxyarginine is not relevant to the mechanism

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The ferrous-dioxy complex of neuronal nitric oxide synthase. Divergent effects of L-arginine and tetrahydrobiopterin on its stability

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Catalysis by nitric oxide synthase

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Formation of a Pterin Radical in the Reaction of the Heme Domain of Inducible Nitric Oxide Synthase with Oxygen†

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Reactions catalyzed by the heme domain of inducible nitric oxide synthase: evidence for the involvement of tetrahydrobiopterin in electron transfer

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Rapid kinetic studies link tetrahydrobiopterin radical formation to heme-dioxy reduction and arginine hydroxylation in inducible nitric-oxide synthase.

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Low-temperature stabilization and spectroscopic characterization of the dioxygen complex of the ferrous neuronal nitric oxide synthase oxygenase domain.

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Superoxide anion production by the autoxidation of cytochrome P450cam

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Reduced Oxy Intermediate Observed in D251N Cytochrome P450cam†

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The catalytic pathway of cytochrome p450cam at atomic resolution

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Substrate analogue induced changes of the CO-stretching mode in the cytochrome P450cam-carbon monoxide complex

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Characterization of the inducible nitric oxide synthase oxygenase domain identifies a 49 amino acid segment required for subunit dimerization and tetrahydrobiopterin interaction

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Nature of O2 and CO binding to metalloporphyrins and heme proteins

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Crystal structure of the carbon monoxide-substrate-cytochrome P-450CAM ternary complex

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Hydrogen-bonding interactions in the active sites of cytochrome P450cam and its site-directed mutants

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10.1016/S0003-9861(02)00555-6

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